ID A2WDL6_9BURK Unreviewed; 646 AA.
AC A2WDL6;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE SubName: Full=Hemolysin {ECO:0000313|EMBL:EAY70062.1};
GN ORFNames=BDAG_02841 {ECO:0000313|EMBL:EAY70062.1};
OS Burkholderia dolosa AU0158.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=350701 {ECO:0000313|EMBL:EAY70062.1, ECO:0000313|Proteomes:UP000053482};
RN [1] {ECO:0000313|Proteomes:UP000053482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU0158 {ECO:0000313|Proteomes:UP000053482};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E., Brockman W., Rounsley S., Young S., LaButti K., Pushparaj V.,
RA DeCaprio D., Crawford M., Koehrsen M., Engels R., Montgomery P.,
RA Pearson M., Howarth C., Kodira C., Zeng Q., Yandava C., Oleary S.,
RA Alvarado L., Lory S., LiPuma J.;
RT "The Genome Sequence of Burkholderia dolosa (strain AU0158).";
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004948}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CH482381; EAY70062.1; -; Genomic_DNA.
DR AlphaFoldDB; A2WDL6; -.
DR HOGENOM; CLU_423718_0_0_4; -.
DR Proteomes; UP000053482; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR CDD; cd00564; TMP_TenI; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR InterPro; IPR036206; ThiamineP_synth_sf.
DR InterPro; IPR022998; ThiamineP_synth_TenI.
DR PANTHER; PTHR43099:SF5; INTEGRAL MEMBRANE PROTEIN-RELATED; 1.
DR PANTHER; PTHR43099; UPF0053 PROTEIN YRKA; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01595; CNNM; 1.
DR Pfam; PF02581; TMP-TENI; 1.
DR SMART; SM00116; CBS; 2.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF51391; Thiamin phosphate synthase; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51846; CNNM; 1.
PE 4: Predicted;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW ProRule:PRU00703}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW ProRule:PRU01193}; Reference proteome {ECO:0000313|Proteomes:UP000053482};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW ProRule:PRU01193};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW ProRule:PRU01193}.
FT TRANSMEM 87..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..191
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 218..278
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 284..341
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT REGION 416..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 608..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 608..622
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 70258 MW; 085F61E83B3FC3A9 CRC64;
MALNGFFVAA EFGLVKLRTT RVKTLARKHG LRGRILGVVH GRLDAYLSAC QLGITLASLG
LGWIGEPAFA ELIGPLLDLL GVESERVVHL ISLVFAFSLI SFLHIVVGEL APKSMAIRQP
EKVGLWVALP LYAFYWAMYP AIWLLNTSAN AVLRLAGLSA DHGSDAHYST DELKLILRSR
RSTAGGAAQP TRGSYSNDEW NTLAHSLDFS SMTVSDLMRP AHEMIGLRRD LPLPDNMEIV
ARHRFSRYPL FADASRERVF GLIHLKDLLL ARHAGAALDD LSDYVRPVQY VKPDMPALDL
FRRFRKGAPH FALVGNKREK PIGFLTLDNL LGALVGQIHD EFHQGDADWS RLDDGTLMGK
GSLPVVSLEQ ALGIDIDEGR AESRRRAGDP GAERSAVRRA ARVVRSLRRR REEDEWASDR
ARARLSEDDE GKPTNDGLVT ARAMNATLPR CCVITPEPAS ASAADCRAFV DRLEAVLARG
DTLVQLRAKS LDAAAFARLA ADALARCDAA GAQLMLNGPI DAAGVMRLDG AGWHLDGAAL
RTVAQRPLPA DTPVSAACHT ADDLLLAARA GADFVTLSPV RPTLSHPGAP TLGWEKFDAL
GRAGRDARLR ARRDDARASR RRASASRIRN RGYSRVLVSR GAAARG
//